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Phosphate-binding protein PstS 1 (PBP 1) (PhoS1) (PstS-1) (38-kDa glycolipoprotein) (38-kDa lipoprotein) (P38) (Antigen Ag78) (Protein antigen B) (Pab)

 PSTS1_MYCTU             Reviewed;         374 AA.
P9WGU1; L0T854; O05868; P15712;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
07-JUN-2017, entry version 28.
RecName: Full=Phosphate-binding protein PstS 1;
Short=PBP 1;
Short=PhoS1 {ECO:0000303|PubMed:19362712};
Short=PstS-1;
AltName: Full=38-kDa glycolipoprotein {ECO:0000303|PubMed:16622205};
AltName: Full=38-kDa lipoprotein {ECO:0000303|PubMed:1906192};
Short=P38;
AltName: Full=Antigen Ag78;
AltName: Full=Protein antigen B {ECO:0000303|PubMed:2545626};
Short=Pab {ECO:0000303|PubMed:2545626};
Flags: Precursor;
Name=pstS1; Synonyms=phoS1; OrderedLocusNames=Rv0934;
ORFNames=MTCY08D9.05c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2545626;
Andersen A.B., Hansen E.B.;
"Structure and mapping of antigenic domains of protein antigen b, a
38,000-molecular-weight protein of Mycobacterium tuberculosis.";
Infect. Immun. 57:2481-2488(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[3]
FUNCTION IN INFECTION, SUBCELLULAR LOCATION, AND PALMITOYLATION.
STRAIN=H37Rv;
PubMed=1906192; DOI=10.1016/0923-2508(91)90097-T;
Young D.B., Garbe T.R.;
"Lipoprotein antigens of Mycobacterium tuberculosis.";
Res. Microbiol. 142:55-65(1991).
[4]
FUNCTION, AND PHOSPHATE-BINDING.
STRAIN=H37Rv;
PubMed=8294447;
Chang Z., Choudhary A., Lathigra R., Quiocho F.A.;
"The immunodominant 38-kDa lipoprotein antigen of Mycobacterium
tuberculosis is a phosphate-binding protein.";
J. Biol. Chem. 269:1956-1958(1994).
[5]
SUBCELLULAR LOCATION, AND INDUCTION BY PHOSPHATE STARVATION.
STRAIN=H37Rv;
PubMed=1612766;
Espitia C., Elinos M., Hernandez-Pando R., Mancilla R.;
"Phosphate starvation enhances expression of the immunodominant 38-
kilodalton protein antigen of Mycobacterium tuberculosis:
demonstration by immunogold electron microscopy.";
Infect. Immun. 60:2998-3001(1992).
[6]
SUBCELLULAR LOCATION.
STRAIN=H37Rv;
PubMed=10426995; DOI=10.1126/science.285.5428.732;
Brightbill H.D., Libraty D.H., Krutzik S.R., Yang R.B., Belisle J.T.,
Bleharski J.R., Maitland M., Norgard M.V., Plevy S.E., Smale S.T.,
Brennan P.J., Bloom B.R., Godowski P.J., Modlin R.L.;
"Host defense mechanisms triggered by microbial lipoproteins through
Toll-like receptors.";
Science 285:732-736(1999).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=15731097; DOI=10.1128/IAI.73.3.1898-1902.2005;
Peirs P., Lefevre P., Boarbi S., Wang X.M., Denis O., Braibant M.,
Pethe K., Locht C., Huygen K., Content J.;
"Mycobacterium tuberculosis with disruption in genes encoding the
phosphate binding proteins PstS1 and PstS2 is deficient in phosphate
uptake and demonstrates reduced in vivo virulence.";
Infect. Immun. 73:1898-1902(2005).
[8]
FUNCTION IN INFECTION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=16622205; DOI=10.1128/IAI.74.5.2686-2696.2006;
Jung S.B., Yang C.S., Lee J.S., Shin A.R., Jung S.S., Son J.W.,
Harding C.V., Kim H.J., Park J.K., Paik T.H., Song C.H., Jo E.K.;
"The mycobacterial 38-kilodalton glycolipoprotein antigen activates
the mitogen-activated protein kinase pathway and release of
proinflammatory cytokines through Toll-like receptors 2 and 4 in human
monocytes.";
Infect. Immun. 74:2686-2696(2006).
[9]
FUNCTION IN INFECTION.
STRAIN=H37Rv;
PubMed=19140873; DOI=10.1111/j.1365-3083.2008.02193.x;
Sanchez A., Espinosa P., Esparza M.A., Colon M., Bernal G.,
Mancilla R.;
"Mycobacterium tuberculosis 38-kDa lipoprotein is apoptogenic for
human monocyte-derived macrophages.";
Scand. J. Immunol. 69:20-28(2009).
[10]
FUNCTION IN INFECTION.
STRAIN=H37Rv;
PubMed=19362712; DOI=10.1016/j.cellimm.2009.03.008;
Drage M.G., Pecora N.D., Hise A.G., Febbraio M., Silverstein R.L.,
Golenbock D.T., Boom W.H., Harding C.V.;
"TLR2 and its co-receptors determine responses of macrophages and
dendritic cells to lipoproteins of Mycobacterium tuberculosis.";
Cell. Immunol. 258:29-37(2009).
[11]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=20933472; DOI=10.1016/j.tube.2010.09.004;
Vanzembergh F., Peirs P., Lefevre P., Celio N., Mathys V., Content J.,
Kalai M.;
"Effect of PstS sub-units or PknD deficiency on the survival of
Mycobacterium tuberculosis.";
Tuberculosis 90:338-345(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[13]
BIOTECHNOLOGY.
PubMed=23719937; DOI=10.1002/eji.201243245;
Palma C., Schiavoni G., Abalsamo L., Mattei F., Piccaro G.,
Sanchez M., Fernandez C., Singh M., Gabriele L.;
"Mycobacterium tuberculosis PstS1 amplifies IFN-gamma and induces IL-
17/IL-22 responses by unrelated memory CD4+ T cells via dendritic cell
activation.";
Eur. J. Immunol. 43:2386-2397(2013).
[14]
FUNCTION IN INFECTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
STRAIN=H37Rv;
PubMed=25359607; DOI=10.1111/sji.12249;
Esparza M., Palomares B., Garcia T., Espinosa P., Zenteno E.,
Mancilla R.;
"PstS-1, the 38-kDa Mycobacterium tuberculosis glycoprotein, is an
adhesin, which binds the macrophage mannose receptor and promotes
phagocytosis.";
Scand. J. Immunol. 81:46-55(2015).
[15]
FUNCTION IN INFECTION.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=25544271; DOI=10.1007/s10495-014-1080-2;
Lim Y.J., Choi J.A., Lee J.H., Choi C.H., Kim H.J., Song C.H.;
"Mycobacterium tuberculosis 38-kDa antigen induces endoplasmic
reticulum stress-mediated apoptosis via toll-like receptor 2/4.";
Apoptosis 20:358-370(2015).
[16]
REVIEW.
PubMed=20234378; DOI=10.1038/nrmicro2321;
Harding C.V., Boom W.H.;
"Regulation of antigen presentation by Mycobacterium tuberculosis: a
role for Toll-like receptors.";
Nat. Rev. Microbiol. 8:296-307(2010).
[17]
X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 25-374 IN COMPLEX WITH
PHOSPHATE.
STRAIN=H37Rv;
PubMed=12842040; DOI=10.1016/S0969-2126(03)00109-6;
Vyas N.K., Vyas M.N., Quiocho F.A.;
"Crystal structure of M tuberculosis ABC phosphate transport receptor:
specificity and charge compensation dominated by ion-dipole
interactions.";
Structure 11:765-774(2003).
-!- FUNCTION: Functions in inorganic phosphate uptake, although
probably not the main uptake protein under phosphate starvation
(PubMed:15731097, PubMed:20933472). Binds phosphate; probably able
to bind both H(2)PO(4)(-) and HPO(4)(2-) (PubMed:8294447,
PubMed:12842040). Part of the ABC transporter complex PstSACB
involved in phosphate import (Probable).
{ECO:0000269|PubMed:12842040, ECO:0000269|PubMed:15731097,
ECO:0000269|PubMed:20933472, ECO:0000269|PubMed:8294447,
ECO:0000305}.
-!- FUNCTION: A host TLR2 agonist (toll-like receptor), shown
experimentally for human and mouse (PubMed:1906192,
PubMed:19362712). Requires both host TLR1 and TLR2 as coreceptors
to elicit host response in mouse (TLR6 may also play a role)
neither CD14 or CD36 function as accessory receptors
(PubMed:19362712). Protein purified from culture filtrate induces
host (human) monocytes to produce TNF-alpha, IL-6 and IL-12 p40
(IL12B) via ERK1/2 (MAPK3 and MAPK1) and p38 MAPK pathways; MEK
inhibitors U0126 and PD98059 and p38 inhibitor SB203580 block most
cytokine production (PubMed:16622205). Host ERK1/2 and p38 MAPK
activation is mediated mainly by TLR2, but also partially by TLR4,
and unlike the case for lipoprotein LpqH the protein moiety of
PstS1 seems to be the antigenic agent (PubMed:16622205). Greater
activation of ERK1/2 and p38 MAPK is seen in patients with active
pulmonary tuberculosis than in tuberculin-negative patients
(PubMed:16622205). Induces apoptosis when incubated with human
monocyte-derived macrophages via TLR2 (PubMed:19140873). Protein
purified from culture filtrate acts via TLR2 and TLR4 to induce
host macrophage (shown for mouse) endoplasmic reticulum stress-
mediated apoptosis via MAPK (at least JNK), C-C motif chemokine 2
(MCP-1, Ccl2) and ZC3H12 endoribonucleases (MCPIP, Zc3h12)
(PubMed:25544271). Functions as an adhesin, binds to human and
mouse macrophages via mannose residues, binds to the mouse
macrophage mannose receptor (possibly Mrc1) and mediates bacterial
phagocytosis (PubMed:25359607). {ECO:0000269|PubMed:16622205,
ECO:0000269|PubMed:1906192, ECO:0000269|PubMed:19140873,
ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:25359607,
ECO:0000269|PubMed:25544271}.
-!- SUBUNIT: The ABC transporter complex is composed of two ATP-
binding proteins (PstB), two transmembrane proteins (PstC and
PstA) and a solute-binding protein (PstS). {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305|PubMed:1906192}. Cell surface
{ECO:0000269|PubMed:1612766, ECO:0000269|PubMed:25359607}.
Secreted, cell wall {ECO:0000269|PubMed:10426995}. Secreted
{ECO:0000305|PubMed:16622205, ECO:0000305|PubMed:1906192}. Note=A
soluble cell wall-associated protein (PubMed:10426995). Also found
in culture filtrate in increasing quantities during growth
(PubMed:1906192, PubMed:16622205). {ECO:0000269|PubMed:10426995,
ECO:0000269|PubMed:16622205, ECO:0000269|PubMed:1906192}.
-!- INDUCTION: Transcription slightly induced by phosphate starvation,
part of the pstB3-pstS2-pstC1-pstA2 operon (PubMed:20933472).
Strongly induced by phosphate starvation (at protein level)
(PubMed:1612766). Also shown to be only slightly induced by
phosphate starvation; results may depend on growth media (at
protein level) (PubMed:20933472). {ECO:0000269|PubMed:1612766,
ECO:0000269|PubMed:20933472}.
-!- PTM: Glycosylated, probably with mannose residues; treatment with
alpha-D-mannosidase abolishes its interaction with concanavalin A.
{ECO:0000269|PubMed:25359607}.
-!- DISRUPTION PHENOTYPE: No growth phenotype in phosphate-rich medium
(3.6 mM Pi), decreased phosphate uptake in phosphate-depleted
medium (PubMed:15731097). Grows faster than wild-type in
restricted (Sauton) phosphate-free medium, even after nutrient
starvation (PubMed:20933472). Decreased growth in infected BALB/c
and C57BL/6 mice for up to 5 months after infection
(PubMed:15731097). {ECO:0000269|PubMed:15731097,
ECO:0000269|PubMed:20933472}.
-!- BIOTECHNOLOGY: When used as a vaccine has immunostimulatory
properties; it stimulates the differentiation of unrelated antigen
memory CD4+ T-cells to produce IFN-gamma, IL-17 and IL-22.
{ECO:0000269|PubMed:23719937}.
-!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M30046; AAA25374.1; -; Genomic_DNA.
EMBL; AL123456; CCP43682.1; -; Genomic_DNA.
PIR; F70584; F70584.
RefSeq; WP_003900236.1; NZ_KK339370.1.
RefSeq; YP_177770.1; NC_000962.3.
PDB; 1PC3; X-ray; 2.16 A; A/B=25-374.
PDBsum; 1PC3; -.
ProteinModelPortal; P9WGU1; -.
SMR; P9WGU1; -.
STRING; 83332.Rv0934; -.
PaxDb; P9WGU1; -.
EnsemblBacteria; CCP43682; CCP43682; Rv0934.
GeneID; 885724; -.
KEGG; mtu:Rv0934; -.
TubercuList; Rv0934; -.
eggNOG; ENOG4107RBH; Bacteria.
eggNOG; COG0226; LUCA.
KO; K02040; -.
OMA; GSGTTYH; -.
PhylomeDB; P9WGU1; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0042301; F:phosphate ion binding; IDA:MTBBASE.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0016036; P:cellular response to phosphate starvation; IEP:MTBBASE.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:InterPro.
GO; GO:0006817; P:phosphate ion transport; IMP:MTBBASE.
InterPro; IPR005673; ABC_phos-bd_PstS.
InterPro; IPR024370; PBP_domain.
Pfam; PF12849; PBP_like_2; 1.
PIRSF; PIRSF002756; PstS; 1.
TIGRFAMs; TIGR00975; 3a0107s03; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell membrane; Cell wall;
Complete proteome; Glycoprotein; Lipoprotein; Membrane; Palmitate;
Phosphate transport; Reference proteome; Secreted; Signal; Transport;
Virulence.
SIGNAL 1 23 {ECO:0000255|PROSITE-ProRule:PRU00303}.
CHAIN 24 374 Phosphate-binding protein PstS 1.
/FTId=PRO_0000031854.
REGION 58 60 Phosphate binding.
{ECO:0000269|PubMed:12842040}.
REGION 185 191 Phosphate binding.
{ECO:0000269|PubMed:12842040}.
BINDING 88 88 Phosphate. {ECO:0000269|PubMed:12842040}.
BINDING 106 106 Phosphate. {ECO:0000269|PubMed:12842040}.
LIPID 24 24 N-palmitoyl cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303,
ECO:0000305|PubMed:1906192}.
LIPID 24 24 S-diacylglycerol cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
STRAND 51 57 {ECO:0000244|PDB:1PC3}.
TURN 59 61 {ECO:0000244|PDB:1PC3}.
HELIX 62 75 {ECO:0000244|PDB:1PC3}.
STRAND 79 82 {ECO:0000244|PDB:1PC3}.
HELIX 88 96 {ECO:0000244|PDB:1PC3}.
STRAND 101 107 {ECO:0000244|PDB:1PC3}.
HELIX 111 116 {ECO:0000244|PDB:1PC3}.
STRAND 120 134 {ECO:0000244|PDB:1PC3}.
HELIX 147 154 {ECO:0000244|PDB:1PC3}.
HELIX 164 169 {ECO:0000244|PDB:1PC3}.
STRAND 184 187 {ECO:0000244|PDB:1PC3}.
HELIX 190 202 {ECO:0000244|PDB:1PC3}.
TURN 204 211 {ECO:0000244|PDB:1PC3}.
STRAND 214 216 {ECO:0000244|PDB:1PC3}.
HELIX 230 240 {ECO:0000244|PDB:1PC3}.
STRAND 244 249 {ECO:0000244|PDB:1PC3}.
HELIX 250 252 {ECO:0000244|PDB:1PC3}.
HELIX 253 258 {ECO:0000244|PDB:1PC3}.
STRAND 265 267 {ECO:0000244|PDB:1PC3}.
HELIX 278 285 {ECO:0000244|PDB:1PC3}.
TURN 286 290 {ECO:0000244|PDB:1PC3}.
STRAND 312 322 {ECO:0000244|PDB:1PC3}.
HELIX 326 339 {ECO:0000244|PDB:1PC3}.
HELIX 342 344 {ECO:0000244|PDB:1PC3}.
HELIX 346 349 {ECO:0000244|PDB:1PC3}.
TURN 350 353 {ECO:0000244|PDB:1PC3}.
HELIX 359 369 {ECO:0000244|PDB:1PC3}.
SEQUENCE 374 AA; 38243 MW; 6334968191FF38AA CRC64;
MKIRLHTLLA VLTAAPLLLA AAGCGSKPPS GSPETGAGAG TVATTPASSP VTLAETGSTL
LYPLFNLWGP AFHERYPNVT ITAQGTGSGA GIAQAAAGTV NIGASDAYLS EGDMAAHKGL
MNIALAISAQ QVNYNLPGVS EHLKLNGKVL AAMYQGTIKT WDDPQIAALN PGVNLPGTAV
VPLHRSDGSG DTFLFTQYLS KQDPEGWGKS PGFGTTVDFP AVPGALGENG NGGMVTGCAE
TPGCVAYIGI SFLDQASQRG LGEAQLGNSS GNFLLPDAQS IQAAAAGFAS KTPANQAISM
IDGPAPDGYP IINYEYAIVN NRQKDAATAQ TLQAFLHWAI TDGNKASFLD QVHFQPLPPA
VVKLSDALIA TISS


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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